RBGP1_MOUSE
ID RBGP1_MOUSE Reviewed; 1064 AA.
AC A2AWA9; Q5DTN1; Q8BQ32; Q8C8W3; Q8CD74; Q8R312;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Rab GTPase-activating protein 1;
DE AltName: Full=GAP and centrosome-associated protein;
DE AltName: Full=Rab6 GTPase-activating protein GAPCenA;
GN Name=Rabgap1 {ECO:0000312|MGI:MGI:2385139};
GN Synonyms=Kiaa4104 {ECO:0000312|EMBL:BAD90509.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC31880.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 646-1064 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC31880.1};
RC TISSUE=Embryonic spinal ganglion {ECO:0000312|EMBL:BAC34703.1},
RC Embryonic testis {ECO:0000312|EMBL:BAC27344.1}, and
RC Retina {ECO:0000312|EMBL:BAC31880.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAD90509.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain {ECO:0000312|EMBL:BAD90509.1};
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH26862.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 733-1064 (ISOFORM 1).
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH26862.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH31714.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH31714.1}, and
RC Mammary tumor {ECO:0000312|EMBL:AAH26862.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-355 AND THR-991, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May act as a GTPase-activating protein of RAB6A. May play a
CC role in microtubule nucleation by centrosome. May participate in a
CC RAB6A-mediated pathway involved in the metaphase-anaphase transition
CC (By similarity). {ECO:0000250|UniProtKB:Q9Y3P9}.
CC -!- SUBUNIT: Interacts with RAB6A and tubulin gamma.
CC {ECO:0000250|UniProtKB:Q9Y3P9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9Y3P9}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y3P9}.
CC Note=Predominantly cytosolic but also associated with the centrosome.
CC {ECO:0000250|UniProtKB:Q9Y3P9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|Ref.2};
CC IsoId=A2AWA9-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=A2AWA9-2; Sequence=VSP_052520, VSP_052521;
CC Name=3 {ECO:0000269|PubMed:16141072};
CC IsoId=A2AWA9-3; Sequence=VSP_052516, VSP_052517, VSP_052518,
CC VSP_052519;
CC -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC insert in Rab's active site. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26862.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH31714.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC34703.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD90509.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK031315; BAC27344.1; -; mRNA.
DR EMBL; AK044346; BAC31880.1; -; mRNA.
DR EMBL; AK051644; BAC34703.1; ALT_INIT; mRNA.
DR EMBL; AK220489; BAD90509.1; ALT_INIT; mRNA.
DR EMBL; AL953890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026862; AAH26862.1; ALT_INIT; mRNA.
DR EMBL; BC031714; AAH31714.1; ALT_INIT; mRNA.
DR CCDS; CCDS16002.1; -. [A2AWA9-1]
DR CCDS; CCDS16003.1; -. [A2AWA9-2]
DR RefSeq; NP_001029132.1; NM_001033960.1. [A2AWA9-2]
DR RefSeq; NP_666233.2; NM_146121.2. [A2AWA9-1]
DR RefSeq; XP_006498057.1; XM_006497994.3.
DR RefSeq; XP_017172964.1; XM_017317475.1.
DR AlphaFoldDB; A2AWA9; -.
DR SMR; A2AWA9; -.
DR BioGRID; 230687; 6.
DR IntAct; A2AWA9; 1.
DR STRING; 10090.ENSMUSP00000068835; -.
DR iPTMnet; A2AWA9; -.
DR PhosphoSitePlus; A2AWA9; -.
DR EPD; A2AWA9; -.
DR MaxQB; A2AWA9; -.
DR PaxDb; A2AWA9; -.
DR PeptideAtlas; A2AWA9; -.
DR PRIDE; A2AWA9; -.
DR ProteomicsDB; 300311; -. [A2AWA9-1]
DR ProteomicsDB; 300312; -. [A2AWA9-2]
DR ProteomicsDB; 300313; -. [A2AWA9-3]
DR Antibodypedia; 30396; 264 antibodies from 27 providers.
DR DNASU; 227800; -.
DR Ensembl; ENSMUST00000061179; ENSMUSP00000061624; ENSMUSG00000035437. [A2AWA9-1]
DR Ensembl; ENSMUST00000066055; ENSMUSP00000068835; ENSMUSG00000035437. [A2AWA9-2]
DR Ensembl; ENSMUST00000112920; ENSMUSP00000108542; ENSMUSG00000035437. [A2AWA9-1]
DR GeneID; 227800; -.
DR KEGG; mmu:227800; -.
DR UCSC; uc008jmw.1; mouse. [A2AWA9-3]
DR UCSC; uc008jmx.1; mouse. [A2AWA9-1]
DR UCSC; uc008jmy.1; mouse. [A2AWA9-2]
DR CTD; 23637; -.
DR MGI; MGI:2385139; Rabgap1.
DR VEuPathDB; HostDB:ENSMUSG00000035437; -.
DR eggNOG; KOG1102; Eukaryota.
DR GeneTree; ENSGT00940000157216; -.
DR HOGENOM; CLU_007394_0_0_1; -.
DR InParanoid; A2AWA9; -.
DR OMA; KPSQGDC; -.
DR PhylomeDB; A2AWA9; -.
DR TreeFam; TF317184; -.
DR BRENDA; 2.3.1.23; 3474.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR BioGRID-ORCS; 227800; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Rabgap1; mouse.
DR PRO; PR:A2AWA9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AWA9; protein.
DR Bgee; ENSMUSG00000035437; Expressed in undifferentiated genital tubercle and 245 other tissues.
DR ExpressionAtlas; A2AWA9; baseline and differential.
DR Genevisible; A2AWA9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR033185; RabGAP1.
DR PANTHER; PTHR22957:SF439; PTHR22957:SF439; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton;
KW GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..1064
FT /note="Rab GTPase-activating protein 1"
FT /id="PRO_0000298780"
FT DOMAIN 137..293
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 561..747
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 805..1038
FT /evidence="ECO:0000255"
FT COMPBIAS 9..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 603
FT /note="Arginine finger"
FT /evidence="ECO:0000250"
FT SITE 644
FT /note="Glutamine finger"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 991
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..18
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052516"
FT VAR_SEQ 19..30
FT /note="TLNSEDFVLVSR -> MGLSSLSANKPW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052517"
FT VAR_SEQ 363..384
FT /note="ESMGKSSDGKSYVITGSWNPKS -> VRFCCCCCCGLFWLWLVFIRNL (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052518"
FT VAR_SEQ 385..1064
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052519"
FT VAR_SEQ 804..809
FT /note="ISQKKL -> VQQRLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052520"
FT VAR_SEQ 810..1064
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052521"
FT CONFLICT 646
FT /note="Q -> E (in Ref. 1; BAC34703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1064 AA; 120798 MW; 8AFAB7C7827F0040 CRC64;
MDDKASVGKI SVSSDSVSTL NSEDFVLVSR QGDETPSTNN GSDDEKTGLK IVGNGSEQQL
QKELADVLMD PPMDDQPGER SQLDGEGDGP LSNQLSASST INPVPLVGLP KPEMSLPVKP
GQGDSEVSSP FTPVADEDSV VFNKLTYLGC ASVNAPRSEV EALRMMSILR SQCQISLDVT
LSVPNVSEGT VRLLDPQTNT EIANYPIYKI LFCVRGHDGT PESDCFAFTE SHYNAELFRI
HVFRCEIQEA VSRILYSFAT AFRRSAKQTP LSATAAPQTP DSDIFTFSVS LEIKEDDGKG
YFSAVPKDKD RQCFKLRQGI DKKIVICVQQ TANKELAIER CFGLLLSPGK DVRNSDMHLL
DLESMGKSSD GKSYVITGSW NPKSPHFQVV NEETPKDKVL FMTTAVDLVI TEVQEPVRFL
LETKVRVCSP NERLFWPFSK RSTTENFFLK LKQIKQKEKK NNADTLYEVV CLESESERER
RKTTASPSVR LPQSGSQSSM IPSPPEDDEE EDNDEPLLSG FGDVSKECAE KILETWGELL
SKWHLNLSVR PKQLSSLVRS GVPEALRGEV WQLLAGCHNN DHLVEKYRIL ITKESPQDSA
ITRDINRTFP AHDYFKDTGG DGQDSLYKIC KAYSVYDEEI GYCQGQSFLA AVLLLHMPEE
QAFSVLVKIM FDYGLRELFK QNFEDLHCKF YQLERLMQEY IPDLYNHFLD ISLEAHMYAS
QWFLTLFTAK FPLYMVFHII DLLLCEGISV IFNVALGLLK TSKDDLLLTD FEGALKFFRV
QLPKRYRSEE NAKRLMELAC NTKISQKKLK KFEKEYHTMR EQQAQQEDPI ERFERENRRL
QEANMRLEQE NDDLAHELVT SKIALRKDLD NAEEKADALN KELLMTKQKL IDAEDEKRRL
EEESAQLKEM CRRELDKAES EIKKNSSIIG DYKQICSQLS ERLEKQQTAN KVEIEKIRQK
VDDCDRCRDF FNKEGRVKGI SSAKGVSDED TDEEKETLKN QLREMELELA QTKLQLVEAE
CKIQDLEHHL GLALSEVQAA KKTWFNRTLS SIKTATGVQG KETC
